SitesBLAST
Comparing 201943 FitnessBrowser__MR1:201943 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5wuwA Serratia marcescens short-chain dehydrogenase/reductase f98l/f202l mutant (see paper)
68% identity, 96% coverage: 12:254/254 of query aligns to 3:245/245 of 5wuwA
- active site: G16 (= G25), S140 (= S149), Y154 (= Y163), L161 (= L170)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G21), R15 (= R24), I17 (= I26), Y36 (= Y45), A37 (≠ V46), A38 (≠ S47), D63 (= D72), S64 (= S73), N90 (= N99), A91 (= A100), G92 (= G101), Y154 (= Y163), K158 (= K167), G185 (= G194), P186 (= P195), V187 (= V196)
6j7uA Crystal structure of blue fluorescent protein from metagenomic library in complex with NADPH (see paper)
54% identity, 96% coverage: 10:254/254 of query aligns to 1:247/247 of 6j7uA
- active site: G16 (= G25), S142 (= S149), Y156 (= Y163)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G21), S14 (= S23), R15 (= R24), I17 (= I26), Y36 (= Y45), V37 (= V46), S38 (= S47), S41 (≠ A50), D65 (= D72), S66 (= S73), N92 (= N99), A93 (= A100), G94 (= G101), I115 (≠ T122), G141 (= G148), S142 (= S149), Y156 (= Y163), K160 (= K167), P186 (= P193), T191 (= T198), M193 (= M200), N194 (= N201)
5u2wA Crystal structure of a short chain dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP
52% identity, 96% coverage: 10:254/254 of query aligns to 2:246/246 of 5u2wA
- active site: G17 (= G25), S141 (= S149), M152 (≠ G160), Y155 (= Y163), K159 (= K167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G21), S15 (= S23), R16 (= R24), G17 (= G25), I18 (= I26), Y37 (= Y45), E38 (≠ V46), K39 (≠ S47), S40 (= S48), A63 (= A71), D64 (= D72), S65 (= S73), N91 (= N99), A92 (= A100), G93 (= G101), T139 (≠ I147), Y155 (= Y163), K159 (= K167), P185 (= P193), G186 (= G194), T188 (≠ V196), T190 (= T198), M192 (= M200), N193 (= N201)
5z2lK Crystal structure of bdca in complex with NADPH (see paper)
45% identity, 96% coverage: 12:254/254 of query aligns to 3:236/244 of 5z2lK
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S14 (= S23), R15 (= R24), I17 (= I26), Y36 (= Y45), A37 (≠ V46), G38 (≠ S47), S39 (= S48), T57 (≠ A71), D58 (= D72), S59 (= S73), N81 (= N99), A82 (= A100), G83 (= G101), I129 (= I147), S131 (= S149), Y145 (= Y163), K149 (= K167), P175 (= P193), I178 (≠ V196), T180 (= T198), A182 (≠ M200), N183 (= N201)
P39333 Cyclic-di-GMP-binding biofilm dispersal mediator protein from Escherichia coli (strain K12) (see paper)
45% identity, 96% coverage: 12:254/254 of query aligns to 4:237/237 of P39333
- E50 (= E58) mutation E->Q,V: Shows higher affinity for cyclic-di-GMP, increases swimming motility and biofilm dispersal. Biofilm formation is almost completely removed.
7yb2D Crystal structure of anthrol reductase (cbar) in complex with NADP+ and emodin (see paper)
37% identity, 94% coverage: 12:251/254 of query aligns to 10:262/264 of 7yb2D
- binding 3-methyl-1,6,8-trihydroxyanthraquinone: S147 (= S149), Y161 (= Y163), G193 (≠ P195), M198 (= M200), F199 (≠ N201), V202 (vs. gap), S203 (vs. gap), Y206 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G21), R22 (= R24), G23 (= G25), I24 (= I26), Y43 (= Y45), A44 (≠ V46), N45 (≠ S47), S46 (= S48), D70 (= D72), V71 (≠ S73), N97 (= N99), S98 (≠ A100), L120 (≠ T122), T145 (≠ I147), S147 (= S149), Y161 (= Y163), K165 (= K167), P191 (= P193), G192 (= G194), T194 (≠ V196), T196 (= T198), M198 (= M200)
8hfkA Crystal structure of cbar mutant (h162f) in complex with NADP+ and halogenated aryl ketone (see paper)
38% identity, 94% coverage: 12:251/254 of query aligns to 6:257/259 of 8hfkA
- binding 2-bromanyl-1-(4-bromanyl-2-oxidanyl-phenyl)ethanone: S143 (≠ T150), N144 (= N151), T145 (≠ A152), F153 (≠ G160), Y156 (= Y163), G187 (= G194), M193 (= M200), V197 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G21), R18 (= R24), I20 (= I26), A40 (≠ V46), N41 (≠ S47), S42 (= S48), D66 (= D72), N93 (= N99), S94 (≠ A100), L116 (≠ T122), T141 (≠ G148), Y156 (= Y163), K160 (= K167), P186 (= P193), G187 (= G194), G188 (≠ P195), T189 (≠ V196), T191 (= T198), M193 (= M200)
Sites not aligning to the query:
8hfjC Crystal structure of cbar mutant (h162f) in complex with NADP+ and a bulky 1,3-cyclodiketone (see paper)
37% identity, 94% coverage: 12:251/254 of query aligns to 6:258/260 of 8hfjC
- binding 2-methyl-2-[(4-methylphenyl)methyl]cyclopentane-1,3-dione: N144 (≠ T150), T145 (≠ N151), F154 (≠ G160), G189 (≠ P195), V198 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G21), R18 (= R24), I20 (= I26), Y39 (= Y45), A40 (≠ V46), N41 (≠ S47), S42 (= S48), D66 (= D72), V67 (≠ S73), N93 (= N99), S94 (≠ A100), L116 (≠ T122), T141 (≠ I147), Y157 (= Y163), K161 (= K167), P187 (= P193), T190 (≠ V196), T192 (= T198), M194 (= M200)
Sites not aligning to the query:
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
40% identity, 95% coverage: 11:252/254 of query aligns to 5:240/243 of 4i08A
- active site: G19 (= G25), N113 (= N123), S141 (= S149), Q151 (≠ G160), Y154 (= Y163), K158 (= K167)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G21), S17 (= S23), R18 (= R24), I20 (= I26), T40 (≠ S47), N62 (≠ D72), V63 (≠ S73), N89 (= N99), A90 (= A100), G140 (= G148), S141 (= S149), Y154 (= Y163), K158 (= K167), P184 (= P193), G185 (= G194), T189 (= T198)
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
40% identity, 95% coverage: 11:252/254 of query aligns to 5:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G21), S17 (= S23), R18 (= R24), I20 (= I26), T40 (≠ S47), N62 (≠ D72), V63 (≠ S73), N89 (= N99), A90 (= A100), I92 (= I102), V139 (≠ I147), S141 (= S149), Y154 (= Y163), K158 (= K167), P184 (= P193), G185 (= G194), I187 (≠ V196), T189 (= T198), M191 (= M200)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
38% identity, 96% coverage: 10:253/254 of query aligns to 7:253/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G21), S20 (= S23), K21 (≠ R24), G22 (= G25), I23 (= I26), A43 (≠ V46), S44 (= S47), S45 (= S48), G68 (≠ A71), D69 (= D72), V70 (≠ S73), N96 (= N99), S97 (≠ A100), G98 (= G101), Y100 (≠ L103), I144 (= I147), S146 (= S149), Y159 (= Y163), K163 (= K167), P189 (= P193), G190 (= G194), M191 (≠ P195), I192 (≠ V196), T194 (= T198), G196 (≠ M200), T197 (≠ N201)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S149), Y159 (= Y163), M191 (≠ P195), I202 (vs. gap)
3tzcA Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg)(y155f) from vibrio cholerae (see paper)
39% identity, 95% coverage: 11:252/254 of query aligns to 5:223/224 of 3tzcA
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
34% identity, 96% coverage: 11:253/254 of query aligns to 4:251/261 of 1g6kA
- active site: G18 (= G25), S145 (= S149), Y158 (= Y163), K162 (= K167)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ R24), G18 (= G25), L19 (≠ I26), R39 (≠ V46), D65 (= D72), V66 (≠ S73), N92 (= N99), A93 (= A100), G94 (= G101), M143 (≠ I147), S145 (= S149), Y158 (= Y163), P188 (= P193), G189 (= G194), I191 (≠ V196), T193 (= T198)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
37% identity, 95% coverage: 12:252/254 of query aligns to 4:244/247 of P73574
- A14 (≠ G22) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ V158) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K167) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ P195) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ S207) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
7nm8AAA Antimycin pathway standalone ketoreductase, AntM (see paper)
38% identity, 96% coverage: 9:251/254 of query aligns to 1:247/251 of 7nm8AAA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G21), S15 (= S23), R16 (= R24), G17 (= G25), I18 (= I26), H36 (≠ T44), Y37 (= Y45), G38 (≠ V46), H39 (≠ S47), L65 (vs. gap), N97 (= N99), G99 (= G101), S147 (≠ T150), Y160 (= Y163), K164 (= K167), G191 (= G194), T193 (≠ V196), T195 (= T198)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
34% identity, 96% coverage: 11:253/254 of query aligns to 4:251/261 of P40288
- 11:35 (vs. 18:42, 36% identical) binding NADP(+)
- E96 (≠ L103) mutation E->A,G,K: Heat stable.
- D108 (= D115) mutation to N: Heat stable.
- V112 (≠ I119) mutation to A: Heat stable.
- E133 (vs. gap) mutation to K: Heat stable.
- V183 (= V188) mutation to I: Heat stable.
- P194 (≠ D199) mutation to Q: Heat stable.
- E210 (≠ K212) mutation to K: Heat stable.
- Y217 (≠ R219) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 95% coverage: 11:252/254 of query aligns to 2:241/244 of P0AEK2
- GASR 12:15 (≠ GGSR 21:24) binding NADP(+)
- T37 (≠ S47) binding NADP(+)
- NV 59:60 (≠ DS 72:73) binding NADP(+)
- N86 (= N99) binding NADP(+)
- Y151 (= Y163) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YGMSK 163:167) binding NADP(+)
- A154 (≠ S166) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K167) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V196) binding NADP(+)
- E233 (≠ A244) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
39% identity, 95% coverage: 11:252/254 of query aligns to 1:240/243 of 1q7bA
- active site: G15 (= G25), E101 (≠ D115), S137 (= S149), Q147 (≠ G160), Y150 (= Y163), K154 (= K167)
- binding calcium ion: E232 (≠ A244), T233 (≠ S245)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G21), S13 (= S23), R14 (= R24), T36 (≠ S47), N58 (≠ D72), V59 (≠ S73), N85 (= N99), A86 (= A100), G87 (= G101), I88 (= I102), S137 (= S149), Y150 (= Y163), K154 (= K167), P180 (= P193), G181 (= G194), I183 (≠ V196)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
36% identity, 94% coverage: 15:252/254 of query aligns to 5:244/246 of 3osuA
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
39% identity, 95% coverage: 11:252/254 of query aligns to 1:240/243 of 1q7cA
- active site: G15 (= G25), S137 (= S149), Q147 (≠ G160), F150 (≠ Y163), K154 (= K167)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G21), S13 (= S23), R14 (= R24), A35 (≠ V46), T36 (≠ S47), L57 (≠ A71), N58 (≠ D72), V59 (≠ S73), G87 (= G101), I88 (= I102)
Query Sequence
>201943 FitnessBrowser__MR1:201943
MSELTMKSSNNLQGKVAFVQGGSRGIGAAIVKRLASEGAAVAFTYVSSEAQSQLLVDEVI
AQGGKAIAIKADSTEPEAIRRAIRETKAHLGGLDIVVNNAGILIWDSIENLTLEDWERIV
NTNVRSVFVASQEAALHMNDGGRIINIGSTNAERIPFVGGAIYGMSKSALVGLAKGLARD
LGPRAITVNNIQPGPVDTDMNPDNGDSSEPIKAIGVLGRYGKAEEIASFVAFIAGPEAGY
ITGASLMIDGGFSA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory